Protein exploration Different proteins appear to be very different and may have multiple functions (water soluble antibodies involved in the immune system, insoluble keratin of hair, hooves, feathers, etc). Nevertheless, each consists of amino acid subunits. Approximately 20 different amino acids have similar chemical structures, but because they have different side groups, they behave very differently. Therefore, stitching them in different combinations produces very different proteins.
The purpose of the JAXA LT PCG survey of the Japan Aerospace Exploration Agency is to cultivate high quality protein crystals under microgravity and study the protein structure in detail. These structures are used to develop drugs to explore the mystery of our lives. Protein samples were sent to the International Space Station (ISS) and crystallized using the despreading method at 4 ° C. Results that everyone learned JAXA has developed a new technique to estimate the impurity trapping rate obtained by the ratio of propulsive power of crystals grown on the ground and in space and the diffusion / capture rate of proteins. This technique demonstrates the presence of protein deficient and impurity deficient regions under microgravity conditions with high viscosity and slow diffusion. I am trying to obtain high quality protein crystals using this technology. Our goal is to contribute to meeting the demands of society.
Protein electrophoresis is the process of separating proteins by placing the protein in a gel matrix and then observing the mobility of the protein in the presence of an electric field. The most common technique is sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS - PAGE). In these gels, the fluidity of the protein is a function of the length and charge of the protein. Since proteins are usually folded and amino acids in the polypeptide chain have different charges, it is desirable to compare their sizes by PAGE, so that all proteins in the mixture have the same unit length charge and the same shape is important. This uniform protein shape and charge proportional to size is achieved by the addition of SDS detergent to remove secondary and tertiary protein structures.